메뉴 건너뛰기




Volumn 45, Issue 5, 2017, Pages 2546-2557

Overlapping roles for PARP1 and PARP2 in the recruitment of endogenous XRCC1 and PNKP into oxidized chromatin

Author keywords

[No Author keywords available]

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 2; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE INHIBITOR; SMALL INTERFERING RNA; XRCC1 PROTEIN; CHROMATIN; DNA BINDING PROTEIN; DNA LIGASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PARP1 PROTEIN, HUMAN; PARP2 PROTEIN, HUMAN; PHOSPHOTRANSFERASE; PNKP PROTEIN, HUMAN; X-RAY REPAIR CROSS COMPLEMENTING PROTEIN 1;

EID: 85018262103     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkw1246     Document Type: Article
Times cited : (143)

References (43)
  • 1
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl, T. (1993) Instability and decay of the primary structure of DNA. Nature, 362, 709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 2
    • 48249095920 scopus 로고    scopus 로고
    • Single-strand break repair and genetic disease
    • Caldecott, K.W. (2008) Single-strand break repair and genetic disease. Nat. Rev. Genet., 9, 619-631.
    • (2008) Nat. Rev. Genet. , vol.9 , pp. 619-631
    • Caldecott, K.W.1
  • 3
    • 84902086815 scopus 로고    scopus 로고
    • Protein ADP-ribosylation and the cellular response to DNA strand breaks
    • Caldecott, K.W. (2014) Protein ADP-ribosylation and the cellular response to DNA strand breaks. DNA Repair (Amst), 19, 108-113.
    • (2014) DNA Repair (Amst) , vol.19 , pp. 108-113
    • Caldecott, K.W.1
  • 4
    • 0000102949 scopus 로고
    • Poly(ADP-ribose) polymerase: A molecular nick-sensor
    • de Murcia, G. and Menissier-de Murcia, J. (1994) Poly(ADP-ribose) polymerase: A molecular nick-sensor. Trends Biochem. Sci., 19, 172-176.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 172-176
    • De Murcia, G.1    Menissier-De Murcia, J.2
  • 6
    • 84882724418 scopus 로고    scopus 로고
    • The FHA and BRCT domains recognize ADP-ribosylation during DNA damage response
    • Li, M., Lu, L.-Y., Yang, C.-Y., Wang, S. and Yu, X. (2013) The FHA and BRCT domains recognize ADP-ribosylation during DNA damage response. Genes Dev., 27, 1752-1768.
    • (2013) Genes Dev. , vol.27 , pp. 1752-1768
    • Li, M.1    Lu, L.-Y.2    Yang, C.-Y.3    Wang, S.4    Yu, X.5
  • 8
    • 0041378046 scopus 로고    scopus 로고
    • XRCC1 and DNA strand break repair
    • Caldecott, K.W. (2003) XRCC1 and DNA strand break repair. DNA Repair (Amst), 2, 955-969.
    • (2003) DNA Repair (Amst) , vol.2 , pp. 955-969
    • Caldecott, K.W.1
  • 9
    • 84908593807 scopus 로고    scopus 로고
    • DNA single-strand break repair
    • Caldecott, K.W. (2014) DNA single-strand break repair. Exp. Cell Res., 329, 2-8.
    • (2014) Exp. Cell Res. , vol.329 , pp. 2-8
    • Caldecott, K.W.1
  • 13
    • 0033588161 scopus 로고    scopus 로고
    • Molecular cloning of the human gene, PNKP, encoding a polynucleotide kinase 3-phosphatase and evidence for its role in repair of DNA strand breaks caused by oxidative damage
    • Jilani, A., Ramotar, D., Slack, C., Ong, C., Yang, X.M., Scherer, S.W. and Lasko, D.D. (1999) Molecular cloning of the human gene, PNKP, encoding a polynucleotide kinase 3-phosphatase and evidence for its role in repair of DNA strand breaks caused by oxidative damage. J. Biol. Chem., 274, 24176-24186.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24176-24186
    • Jilani, A.1    Ramotar, D.2    Slack, C.3    Ong, C.4    Yang, X.M.5    Scherer, S.W.6    Lasko, D.D.7
  • 19
    • 0033135769 scopus 로고    scopus 로고
    • A human poly(ADP-ribose) polymerase gene family (ADPRTL): CDNA cloning of two novel poly(ADP-ribose) polymerase homologues
    • Johansson, M. (1999) A human poly(ADP-ribose) polymerase gene family (ADPRTL): CDNA cloning of two novel poly(ADP-ribose) polymerase homologues. Genomics, 57, 442-445.
    • (1999) Genomics , vol.57 , pp. 442-445
    • Johansson, M.1
  • 21
    • 84903977632 scopus 로고    scopus 로고
    • PARP-2 and PARP-3 are selectively activated by 5 phosphorylated DNA breaks through an allosteric regulatory mechanism shared with PARP-1
    • Langelier, M.-F., Riccio, A.A. and Pascal, J.M. (2014) PARP-2 and PARP-3 are selectively activated by 5 phosphorylated DNA breaks through an allosteric regulatory mechanism shared with PARP-1. Nucleic Acids Res., 42, 7762-7775.
    • (2014) Nucleic Acids Res. , vol.42 , pp. 7762-7775
    • Langelier, M.-F.1    Riccio, A.A.2    Pascal, J.M.3
  • 24
    • 0038583869 scopus 로고    scopus 로고
    • Spatial and temporal cellular responses to single-strand breaks in human cells
    • Okano, S., Lan, L., Caldecott, K.W., Mori, T. and Yasui, A. (2003) Spatial and temporal cellular responses to single-strand breaks in human cells. Mol. Cell. Biol., 23, 3974-3981.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3974-3981
    • Okano, S.1    Lan, L.2    Caldecott, K.W.3    Mori, T.4    Yasui, A.5
  • 25
    • 0142009654 scopus 로고    scopus 로고
    • A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage
    • El-Khamisy, S.F., Masutani, M., Suzuki, H. and Caldecott, K.W. (2003) A requirement for PARP-1 for the assembly or stability of XRCC1 nuclear foci at sites of oxidative DNA damage. Nucleic Acids Res., 31, 5526-5533.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5526-5533
    • El-Khamisy, S.F.1    Masutani, M.2    Suzuki, H.3    Caldecott, K.W.4
  • 26
    • 38049007502 scopus 로고    scopus 로고
    • Feedback-regulated poly(ADP-ribosyl)ation by PARP-1 is required for rapid response to DNA damage in living cells
    • Mortusewicz, O., Amé, J.-C., Schreiber, V. and Leonhardt, H. (2007) Feedback-regulated poly(ADP-ribosyl)ation by PARP-1 is required for rapid response to DNA damage in living cells. Nucleic Acids Res., 35, 7665-7675.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 7665-7675
    • Mortusewicz, O.1    Amé, J.-C.2    Schreiber, V.3    Leonhardt, H.4
  • 27
    • 34547225606 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 1 accelerates single-strand break repair in concert with poly(ADP-ribose) glycohydrolase
    • Fisher, A.E.O., Hochegger, H., Takeda, S. and Caldecott, K.W. (2007) Poly(ADP-ribose) polymerase 1 accelerates single-strand break repair in concert with poly(ADP-ribose) glycohydrolase. Mol. Cell. Biol., 27, 5597-5605.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 5597-5605
    • Fisher, A.E.O.1    Hochegger, H.2    Takeda, S.3    Caldecott, K.W.4
  • 28
    • 23244437030 scopus 로고    scopus 로고
    • DNA polymerase beta promotes recruitment of DNA ligase III alpha-XRCC1 to sites of base excision repair
    • Parsons, J.L., Dianova, I.I., Allinson, S.L. and Dianov, G.L. (2005) DNA polymerase beta promotes recruitment of DNA ligase III alpha-XRCC1 to sites of base excision repair. Biochemistry, 44, 10613-10619.
    • (2005) Biochemistry , vol.44 , pp. 10613-10619
    • Parsons, J.L.1    Dianova, I.I.2    Allinson, S.L.3    Dianov, G.L.4
  • 29
    • 28044453306 scopus 로고    scopus 로고
    • End-damage-specific proteins facilitate recruitment or stability of X-ray cross-complementing protein 1 at the sites of DNA single-strand break repair
    • Parsons, J.L., Dianova, I.I., Boswell, E., Weinfeld, M. and Dianov, G.L. (2005) End-damage-specific proteins facilitate recruitment or stability of X-ray cross-complementing protein 1 at the sites of DNA single-strand break repair. FEBS J., 272, 5753-5763.
    • (2005) FEBS J. , vol.272 , pp. 5753-5763
    • Parsons, J.L.1    Dianova, I.I.2    Boswell, E.3    Weinfeld, M.4    Dianov, G.L.5
  • 30
    • 84941095899 scopus 로고    scopus 로고
    • DNA ligase III acts as a DNA strand break sensor in the cellular orchestration of DNA strand break repair
    • Abdou, I., Poirier, G.G., Hendzel, M.J. and Weinfeld, M. (2014) DNA ligase III acts as a DNA strand break sensor in the cellular orchestration of DNA strand break repair. Nucleic Acids Res., 43, 875-892.
    • (2014) Nucleic Acids Res. , vol.43 , pp. 875-892
    • Abdou, I.1    Poirier, G.G.2    Hendzel, M.J.3    Weinfeld, M.4
  • 32
    • 68849105162 scopus 로고    scopus 로고
    • DNA 3-phosphatase activity is critical for rapid global rates of single-strand break repair following oxidative stress
    • Breslin, C. and Caldecott, K.W. (2009) DNA 3-phosphatase activity is critical for rapid global rates of single-strand break repair following oxidative stress.Mol Cell Biol, 29, 4653-4662.
    • (2009) Mol Cell Biol , vol.29 , pp. 4653-4662
    • Breslin, C.1    Caldecott, K.W.2
  • 34
    • 84896929630 scopus 로고    scopus 로고
    • Improving CRISPR-Cas nuclease specificity using truncated guide RNAs
    • Fu, Y., Sander, J.D., Reyon, D., Cascio, V.M. and Joung, J.K. (2014) Improving CRISPR-Cas nuclease specificity using truncated guide RNAs. Nat. Biotechnol., 32, 279-284.
    • (2014) Nat. Biotechnol. , vol.32 , pp. 279-284
    • Fu, Y.1    Sander, J.D.2    Reyon, D.3    Cascio, V.M.4    Joung, J.K.5
  • 35
    • 0018787368 scopus 로고
    • X-ray induced DNA double strand break production and repair in mammalian cells as measured by neutral filter elution
    • Bradley, M.O. and Kohn, K.W. (1979) X-ray induced DNA double strand break production and repair in mammalian cells as measured by neutral filter elution. Nucleic Acids Res., 7, 793-804.
    • (1979) Nucleic Acids Res. , vol.7 , pp. 793-804
    • Bradley, M.O.1    Kohn, K.W.2
  • 36
    • 84892932423 scopus 로고    scopus 로고
    • Emerging roles of the nucleolus in regulating the DNA damage response: The noncanonical DNA repair enzyme APE1/Ref-1 as a paradigmatical example
    • Antoniali, G., Lirussi, L., Poletto, M. and Tell, G. (2014) Emerging roles of the nucleolus in regulating the DNA damage response: The noncanonical DNA repair enzyme APE1/Ref-1 as a paradigmatical example. Antioxid. Redox Signal., 20, 621-639.
    • (2014) Antioxid. Redox Signal. , vol.20 , pp. 621-639
    • Antoniali, G.1    Lirussi, L.2    Poletto, M.3    Tell, G.4
  • 38
    • 59349083787 scopus 로고    scopus 로고
    • Delocalization of nucleolar poly(ADP-ribose) polymerase-1 to the nucleoplasm and its novel link to cellular sensitivity to DNA damage
    • Rancourt, A. and Satoh, M.S. (2009) Delocalization of nucleolar poly(ADP-ribose) polymerase-1 to the nucleoplasm and its novel link to cellular sensitivity to DNA damage. DNA Repair (Amst), 8, 286-297.
    • (2009) DNA Repair (Amst) , vol.8 , pp. 286-297
    • Rancourt, A.1    Satoh, M.S.2
  • 39
    • 27744568392 scopus 로고    scopus 로고
    • BRCA2-deficient CAPAN-1 cells are extremely sensitive to the inhibition of Poly (ADP-Ribose) polymerase: An issue of potency
    • McCabe, N., Lord, C.J., Tutt, A.N.J., Martin, N.M.B., Smith, G.C.M. and Ashworth, A. (2005) BRCA2-deficient CAPAN-1 cells are extremely sensitive to the inhibition of Poly (ADP-Ribose) polymerase: An issue of potency. Cancer Biol. Ther., 4, 934-936.
    • (2005) Cancer Biol. Ther. , vol.4 , pp. 934-936
    • McCabe, N.1    Lord, C.J.2    Tutt, A.N.J.3    Martin, N.M.B.4    Smith, G.C.M.5    Ashworth, A.6
  • 40
    • 47049104588 scopus 로고    scopus 로고
    • APLF (C2orf13) is a novel component of poly(ADP-ribose) signaling in mammalian cells
    • Rulten, S.L., Cortes Ledesma, F., Guo, L., Iles, N.J. and Caldecott, K.W. (2008) APLF (C2orf13) is a novel component of poly(ADP-ribose) signaling in mammalian cells. Mol. Cell. Biol., 28, 4620-4628.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 4620-4628
    • Rulten, S.L.1    Cortes Ledesma, F.2    Guo, L.3    Iles, N.J.4    Caldecott, K.W.5
  • 41
    • 0037151051 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1
    • Schreiber, V., Amé, J.-C., Dollé, P., Schultz, I., Rinaldi, B., Fraulob, V., Ménissier-de Murcia, J. and de Murcia, G. (2002) Poly(ADP-ribose) polymerase-2 (PARP-2) is required for efficient base excision DNA repair in association with PARP-1 and XRCC1. J. Biol. Chem., 277, 23028-23036.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23028-23036
    • Schreiber, V.1    Amé, J.-C.2    Dollé, P.3    Schultz, I.4    Rinaldi, B.5    Fraulob, V.6    Ménissier-De Murcia, J.7    De Murcia, G.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.